1. Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion.
- Author
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Jensen PH, Soroka V, Thomsen NK, Ralets I, Berezin V, Bock E, and Poulsen FM
- Subjects
- Amino Acid Substitution, Binding Sites, Cell Adhesion, Crystallization, Crystallography, X-Ray, Dimerization, Disulfides chemistry, Immunoglobulins chemistry, Models, Molecular, Molecular Sequence Data, Neural Cell Adhesion Molecules genetics, Neural Cell Adhesion Molecules metabolism, Neurons chemistry, Neurons cytology, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments chemistry, Peptide Fragments genetics, Protein Binding, Protein Conformation, Protein Structure, Secondary, Static Electricity, Thermodynamics, Neural Cell Adhesion Molecules chemistry, Neurons physiology, Peptide Fragments metabolism
- Abstract
The structure in solution of the second Ig-module fragment of residues 117-208 of NCAM has been determined. Like the first Ig-module of residues 20-116, it belongs to the I set of the immunogloblin superfamily. Module 1 and module 2 interact weakly, and the binding sites of this interaction have been identified. The two-module fragment NCAM(20-208) is a stable dimer. Removal of the charged residues in these sites in NCAM(20-208) abolishes the dimerization. Modeling the dimer of NCAM(20-208) to fit the interactions of these charges produces one coherent binding site for the formation of two antiparallel strands of the first two NCAM modules. This mode of binding could be a major element in trans-cellular interactions in neural cell adhesion.
- Published
- 1999
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